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</style> | </style> | ||
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$('.sidebar-nav').affix({ | $('.sidebar-nav').affix({ | ||
− | offset: { top: $('. | + | offset: { top: $('.navbar-fixed-top').offset().top } |
}); | }); | ||
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<div class="container"> | <div class="container"> | ||
<div class="row"> | <div class="row"> | ||
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<nav class="col-sm-3" id="side-menu"> | <nav class="col-sm-3" id="side-menu"> | ||
− | <ul class="nav sidebar-nav nav-pills nav-stacked | + | <ul class="nav sidebar-nav nav-pills nav-stacked"> |
<li class="active"><a href="#overview">Overview</a></li> | <li class="active"><a href="#overview">Overview</a></li> | ||
<li><a href="#s-layer">S-layer Engineering</a></li> | <li><a href="#s-layer">S-layer Engineering</a></li> |
Revision as of 21:41, 16 October 2016
Human Practices
Overview
S-layer Engineering
The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent in vitro recrystallization properties on solid supports, SbpA represents a suitable candidate for genetically engineering to create a versatile self-assembly system for the development of a molecular construction kit for nanobiotechnological applications. The first goal of this study was to investigate the surface location of 3 different C-terminal amino acid positions within the S-layer lattice formed by SbpA. Therefore, three derivatives of SbpA were constructed, in